The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure

Chung Ke Chang, Shih Che Sue, Tsan Hung Yu, Chiu Min Hsieh, Cheng Kun Tsai, Yen Chieh Chiang, Shin Jye Lee, Hsin Hao Hsiao, Wen Jin Wu, Chi Fon Chang, Tai Huang Huang

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27 Citations (Scopus)

Abstract

We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five α helices and a β-hairpin. The dimer interface consists of a continuous four-stranded β-sheet superposed by two long α helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the β-sheet and the α helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.

Original languageEnglish
Pages (from-to)5663-5668
Number of pages6
JournalFEBS Letters
Volume579
Issue number25
DOIs
Publication statusPublished - 2005 Oct 24

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Keywords

  • Capsid protein
  • Coronavirus
  • NMR
  • Oligomerization
  • SARS

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Chang, C. K., Sue, S. C., Yu, T. H., Hsieh, C. M., Tsai, C. K., Chiang, Y. C., Lee, S. J., Hsiao, H. H., Wu, W. J., Chang, C. F., & Huang, T. H. (2005). The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure. FEBS Letters, 579(25), 5663-5668. https://doi.org/10.1016/j.febslet.2005.09.038